Conformational changes of active sites during refolding of urea-denatured creatine kinase

Chaperone‐like activity of peptidyl‐prolyl cis‐trans isomerase during creatine kinase refolding

“…Furthermore, Yang et al (1999) verified the existence of a monomeric intermediate in the CK refolding pathway. The present results were combined with those of previous studies (Wang et al 1995;Yang et al 1997Yang et al , 1999 (Freskgard et al 1992).…”

“…(2) Extensively denatured or modified CK can spontaneously refold to its native conformation in vitro (Bickerstaff et al 1980; Hou et al 1983; Grossman 1984; Zhou and Tsou 1986). (3) Because CK is a large dimeric protein, its refolding is much more complicated than molecules that form small dimers or monomers, and involves several intermediates (Zhou and Tsou 1986; Wang et al 1995; Yang et al 1999). The competition between protein aggregation and correct folding has been previously investigated using CK (Webb et al 1997; Zhou et al 1997).…”

“…For in vitro CK folding, completely unfolded CK either correctly folds and forms an active dimer or produces misfolded intermediates and aggregates (side reactions) according to the CK folding pathway proposed by Wang et al (1995). The CK aggregation was described as a nonspecific association through hydrophobic interactions of partially folded polypeptide chains.…”

Chaperone‐like activity of peptidyl‐prolyl cis‐trans isomerase during creatine kinase refolding

“…Furthermore, Yang et al (1999) verified the existence of a monomeric intermediate in the CK refolding pathway. The present results were combined with those of previous studies (Wang et al 1995;Yang et al 1997Yang et al , 1999 (Freskgard et al 1992).…”

“…(2) Extensively denatured or modified CK can spontaneously refold to its native conformation in vitro (Bickerstaff et al 1980; Hou et al 1983; Grossman 1984; Zhou and Tsou 1986). (3) Because CK is a large dimeric protein, its refolding is much more complicated than molecules that form small dimers or monomers, and involves several intermediates (Zhou and Tsou 1986; Wang et al 1995; Yang et al 1999). The competition between protein aggregation and correct folding has been previously investigated using CK (Webb et al 1997; Zhou et al 1997).…”

“…For in vitro CK folding, completely unfolded CK either correctly folds and forms an active dimer or produces misfolded intermediates and aggregates (side reactions) according to the CK folding pathway proposed by Wang et al (1995). The CK aggregation was described as a nonspecific association through hydrophobic interactions of partially folded polypeptide chains.…”

Catalysis of Creatine Kinase Refolding by Protein Disulfide Isomerase Involves Disulfide Cross-link and Dimer to Tetramer Switch

“…According to the unusual experimental observations in this research and our previous work on the folding pathways of CK (14,15,34), a working model was proposed for the molecular mechanism of CK refolding catalyzed by PDI (Scheme I). Previous work showed that the native dimeric CK (N) dissociated to monomers (U) upon denaturation (k dena ).…”

Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

“…Extensive studies have been carried out on CK and monomer AK. The unfolding/refolding of CK in either denaturant solutions [4][5][6][7][8] or thermal denaturation [9,10] were reported previously, as was data for the monomer of AK [11,12]. However, in contrast, little research has been carried out on dimeric AK.…”

Chaperone‐like activity of peptidyl‐prolyl cis‐trans isomerase during creatine kinase refolding

“…Furthermore, Yang et al (1999) verified the existence of a monomeric intermediate in the CK refolding pathway. The present results were combined with those of previous studies (Wang et al 1995;Yang et al 1997Yang et al , 1999 (Freskgard et al 1992).…”

“…(2) Extensively denatured or modified CK can spontaneously refold to its native conformation in vitro (Bickerstaff et al 1980; Hou et al 1983; Grossman 1984; Zhou and Tsou 1986). (3) Because CK is a large dimeric protein, its refolding is much more complicated than molecules that form small dimers or monomers, and involves several intermediates (Zhou and Tsou 1986; Wang et al 1995; Yang et al 1999). The competition between protein aggregation and correct folding has been previously investigated using CK (Webb et al 1997; Zhou et al 1997).…”

“…For in vitro CK folding, completely unfolded CK either correctly folds and forms an active dimer or produces misfolded intermediates and aggregates (side reactions) according to the CK folding pathway proposed by Wang et al (1995). The CK aggregation was described as a nonspecific association through hydrophobic interactions of partially folded polypeptide chains.…”

Catalysis of Creatine Kinase Refolding by Protein Disulfide Isomerase Involves Disulfide Cross-link and Dimer to Tetramer Switch

“…According to the unusual experimental observations in this research and our previous work on the folding pathways of CK (14,15,34), a working model was proposed for the molecular mechanism of CK refolding catalyzed by PDI (Scheme I). Previous work showed that the native dimeric CK (N) dissociated to monomers (U) upon denaturation (k dena ).…”

Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

“…Extensive studies have been carried out on CK and monomer AK. The unfolding/refolding of CK in either denaturant solutions [4][5][6][7][8] or thermal denaturation [9,10] were reported previously, as was data for the monomer of AK [11,12]. However, in contrast, little research has been carried out on dimeric AK.…”

Chaperone‐like activity of peptidyl‐prolyl cis‐trans isomerase during creatine kinase refolding

“…Furthermore, Yang et al (1999) verified the existence of a monomeric intermediate in the CK refolding pathway. The present results were combined with those of previous studies (Wang et al 1995;Yang et al 1997Yang et al , 1999 (Freskgard et al 1992).…”

“…(2) Extensively denatured or modified CK can spontaneously refold to its native conformation in vitro (Bickerstaff et al 1980; Hou et al 1983; Grossman 1984; Zhou and Tsou 1986). (3) Because CK is a large dimeric protein, its refolding is much more complicated than molecules that form small dimers or monomers, and involves several intermediates (Zhou and Tsou 1986; Wang et al 1995; Yang et al 1999). The competition between protein aggregation and correct folding has been previously investigated using CK (Webb et al 1997; Zhou et al 1997).…”

“…For in vitro CK folding, completely unfolded CK either correctly folds and forms an active dimer or produces misfolded intermediates and aggregates (side reactions) according to the CK folding pathway proposed by Wang et al (1995). The CK aggregation was described as a nonspecific association through hydrophobic interactions of partially folded polypeptide chains.…”

Catalysis of Creatine Kinase Refolding by Protein Disulfide Isomerase Involves Disulfide Cross-link and Dimer to Tetramer Switch

“…According to the unusual experimental observations in this research and our previous work on the folding pathways of CK (14,15,34), a working model was proposed for the molecular mechanism of CK refolding catalyzed by PDI (Scheme I). Previous work showed that the native dimeric CK (N) dissociated to monomers (U) upon denaturation (k dena ).…”

Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

“…Extensive studies have been carried out on CK and monomer AK. The unfolding/refolding of CK in either denaturant solutions [4][5][6][7][8] or thermal denaturation [9,10] were reported previously, as was data for the monomer of AK [11,12]. However, in contrast, little research has been carried out on dimeric AK.…”